PAFA_CAVPO
ID PAFA_CAVPO Reviewed; 436 AA.
AC P70683;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Platelet-activating factor acetylhydrolase;
DE Short=PAF acetylhydrolase;
DE EC=3.1.1.47 {ECO:0000250|UniProtKB:Q13093};
DE AltName: Full=1-alkyl-2-acetylglycerophosphocholine esterase;
DE AltName: Full=2-acetyl-1-alkylglycerophosphocholine esterase;
DE AltName: Full=LDL-associated phospholipase A2;
DE Short=LDL-PLA(2);
DE AltName: Full=PAF 2-acylhydrolase;
DE Flags: Precursor;
GN Name=PLA2G7; Synonyms=PAFAH;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Hartley; TISSUE=Liver;
RX PubMed=8947850; DOI=10.1093/oxfordjournals.jbchem.a021488;
RA Karasawa K., Kuge O., Kawasaki K., Nishijima M., Nakano Y., Tomita M.,
RA Yokoyama K., Setaka M., Nojima S.;
RT "Cloning, expression and characterization of plasma platelet-activating
RT factor-acetylhydrolase from guinea pig.";
RL J. Biochem. 120:838-844(1996).
CC -!- FUNCTION: Lipoprotein-associated calcium-independent phospholipase A2
CC involved in phospholipid catabolism during inflammatory and oxidative
CC stress response (By similarity). At the lipid-aqueous interface,
CC hydrolyzes the ester bond of fatty acyl group attached at sn-2 position
CC of phospholipids (phospholipase A2 activity) (By similarity).
CC Specifically targets phospholipids with a short-chain fatty acyl group
CC at sn-2 position. Can hydrolyze phospholipids with long fatty acyl
CC chains, only if they carry oxidized functional groups (By similarity).
CC Hydrolyzes and inactivates platelet-activating factor (PAF, 1-O-alkyl-
CC 2-acetyl-sn-glycero-3-phosphocholine), a potent pro-inflammatory
CC signaling lipid that acts through PTAFR on various innate immune cells
CC (By similarity). Hydrolyzes oxidatively truncated phospholipids
CC carrying an aldehyde group at omega position, preventing their
CC accumulation in lipoprotein particles and uncontrolled pro-inflammatory
CC effects (By similarity). As part of high-density lipoprotein (HDL)
CC particles, can hydrolyze phospholipids having long-chain fatty acyl
CC hydroperoxides at sn-2 position and protect against potential
CC accumulation of these oxylipins in the vascular wall (By similarity).
CC Catalyzes the release from membrane phospholipids of F2-isoprostanes,
CC lipid biomarkers of cellular oxidative damage (By similarity).
CC {ECO:0000250|UniProtKB:Q13093}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC alkyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:17777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:30909, ChEBI:CHEBI:36707; EC=3.1.1.47;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17778;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-decyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC decyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:41376, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:78108, ChEBI:CHEBI:78109;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41377;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-dodecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC dodecyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:41372, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:78103, ChEBI:CHEBI:78104;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41373;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-tetradecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC O-tetradecyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:41368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:78101, ChEBI:CHEBI:78102;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41369;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-octadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC O-octadecyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:41183, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:52450, ChEBI:CHEBI:75216;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41184;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:41203, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:72998, ChEBI:CHEBI:75219;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41204;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-propionyl-sn-glycero-3-phosphocholine + H2O =
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + propanoate;
CC Xref=Rhea:RHEA:41191, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17272, ChEBI:CHEBI:72998, ChEBI:CHEBI:77831;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41192;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-butanoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + butanoate + H(+);
CC Xref=Rhea:RHEA:41195, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17968, ChEBI:CHEBI:72998, ChEBI:CHEBI:77832;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41196;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-pentanoyl-sn-glycero-3-phosphocholine + H2O =
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + pentanoate;
CC Xref=Rhea:RHEA:41199, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:31011, ChEBI:CHEBI:72998, ChEBI:CHEBI:77833;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41200;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-glutaroyl-sn-glycero-3-phosphocholine + H2O =
CC 1-hexadecanoyl-sn-glycero-3-phosphocholine + glutarate + H(+);
CC Xref=Rhea:RHEA:41159, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30921, ChEBI:CHEBI:72998, ChEBI:CHEBI:77756;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41160;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5-oxopentanoyl)-sn-glycero-3-phosphocholine
CC + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 5-oxopentanoate
CC + H(+); Xref=Rhea:RHEA:40483, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16120, ChEBI:CHEBI:72998, ChEBI:CHEBI:77890;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40484;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9-oxononanoyl)-sn-glycero-3-phosphocholine +
CC H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine + 9-oxononanoate +
CC H(+); Xref=Rhea:RHEA:41179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:61042, ChEBI:CHEBI:72998, ChEBI:CHEBI:77812;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41180;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-[9-hydroperoxy-(10E-octadecenoyl)]-sn-
CC glycero-3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + 9-hydroperoxy-10E-octadecenoate + H(+);
CC Xref=Rhea:RHEA:41151, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:77753, ChEBI:CHEBI:77754;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41152;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(10-hydroperoxy-8E-octadecenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = 1-hexadecanoyl-sn-glycero-3-phosphocholine +
CC 10-hydroperoxy-8E-octadecenoate + H(+); Xref=Rhea:RHEA:41155,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:77749, ChEBI:CHEBI:77755;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41156;
CC Evidence={ECO:0000250|UniProtKB:Q13093};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:Q60963}. Note=Associates with HDL particles in
CC plasma. {ECO:0000250|UniProtKB:Q60963}.
CC -!- TISSUE SPECIFICITY: Plasma. {ECO:0000250|UniProtKB:Q13093}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q13093}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D67037; BAA11054.1; -; mRNA.
DR PIR; JC5021; JC5021.
DR RefSeq; NP_001166357.1; NM_001172886.1.
DR RefSeq; XP_005005344.1; XM_005005287.2.
DR RefSeq; XP_013011984.1; XM_013156530.1.
DR RefSeq; XP_013011985.1; XM_013156531.1.
DR AlphaFoldDB; P70683; -.
DR SMR; P70683; -.
DR STRING; 10141.ENSCPOP00000011506; -.
DR ESTHER; cavpo-pafa; PAF-Acetylhydrolase.
DR Ensembl; ENSCPOT00000044445; ENSCPOP00000024215; ENSCPOG00000012786.
DR GeneID; 100135600; -.
DR KEGG; cpoc:100135600; -.
DR CTD; 7941; -.
DR eggNOG; KOG3847; Eukaryota.
DR GeneTree; ENSGT00390000005233; -.
DR HOGENOM; CLU_022501_0_0_1; -.
DR InParanoid; P70683; -.
DR OMA; TYYFQDQ; -.
DR OrthoDB; 1189747at2759; -.
DR TreeFam; TF313831; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000012786; Expressed in liver and 11 other tissues.
DR GO; GO:0034364; C:high-density lipoprotein particle; ISS:UniProtKB.
DR GO; GO:0034362; C:low-density lipoprotein particle; ISS:UniProtKB.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; ISS:UniProtKB.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0034440; P:lipid oxidation; IEA:Ensembl.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IEA:Ensembl.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; ISS:UniProtKB.
DR GO; GO:0034441; P:plasma lipoprotein particle oxidation; IEA:Ensembl.
DR GO; GO:0062234; P:platelet activating factor catabolic process; ISS:UniProtKB.
DR GO; GO:0046469; P:platelet activating factor metabolic process; ISS:UniProtKB.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IEA:Ensembl.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR005065; PAF_acetylhydro-like.
DR InterPro; IPR016715; PAF_acetylhydro_eucaryote.
DR PANTHER; PTHR10272; PTHR10272; 1.
DR Pfam; PF03403; PAF-AH_p_II; 1.
DR PIRSF; PIRSF018169; PAF_acetylhydrolase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; HDL; Hydrolase; Lipid degradation; Lipid metabolism;
KW Phospholipid degradation; Phospholipid metabolism; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250"
FT CHAIN 22..436
FT /note="Platelet-activating factor acetylhydrolase"
FT /id="PRO_0000017832"
FT ACT_SITE 271
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 294
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 349
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 436 AA; 49063 MW; C359D96E392FFE11 CRC64;
MAPPKLHTLF CLSGFLALVH PFDWRDLDPV TYIQSSVWIQ RIQSELLITS FGHTTIPKGN
GPYSVGCTDL MSGYTNQSSF LRLYYPSQDN DFPDALWIPN EEYFQGLTET LGASSFLGKL
LKLLYGSVKV PAKWNSPLKT GEKYPLIIFS HGLGAFRSIY SAIGIELASH GFIVAAVEHR
DESAAATYYF QDAPAAESGN RSWIYYKVGN LETEERKRQL RQRGEECSQA LSWLLSIDEG
EPVKNVLDLN FDIQQLKGSL DRSKVAIIGH SFGGATVIQT LSEDQRFRCG IALDPWMFPV
GEDVHSKIPQ PLFFINSEYF QSANDTKKIE KFYQPQKERK MIAVKGSVHH NFVDFTFATG
KIIGQMLSLK GKIDSEVAMD LINKASLAFL QKYLGLDKNF DQWNSLMEGD DENLIPEFTI
PTTMQSSTGT EQRNPD
